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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
1991-8-14
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pubmed:databankReference |
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pubmed:abstractText |
Several results suggest that P elements have recently invaded natural populations of Drosophila melanogaster after a horizontal transfer from another species. The donor species is thought to come from the willistoni group, which contains P elements very homologous to those of D. melanogaster. However, more divergent P elements are present in many other Drosophilidae species. We have analyzed such elements from Scaptomyza pallida, a species phylogenetically distant to D. melanogaster. We report here the isolation of two coding P elements from S. pallida (PS2 and PS18) that are 4% divergent from one another. At least one of these elements (PS18) is active since it is able to transpose in D. melanogaster and to mobilize a D. melanogaster defective P element, even though its nucleotide sequence is 24% divergent from the canonical P element of D. melanogaster. To our knowledge, a P element that is active and strongly divergent from the D. melanogaster P element has not been reported previously. Sequence comparison between the complete P elements of D. melanogaster and S. pallida reveals that the structural characteristics are maintained: PS2 and PS18 contain terminal inverted repeats and internal repeats very similar to those of the D. melanogaster P element. In addition, the noncoding regions cis necessary for the transposition are more conserved than the coding sequences. Two domains found in the D. melanogaster P transposase (helix-turn-helix and leucine zipper) are well conserved in the putative proteins encoded by PS2 and PS18. This study provides insights into which parts of P elements are functionally important and correlates with functional studies of the P element in D. melanogaster.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-1963871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-1965103,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2155157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2164887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2176696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2416475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2545527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2553268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2558959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2819880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2829216,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2832695,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2838720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2840331,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-2845368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-3018270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-4091267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-6087152,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-6088058,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-6093120,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-6235151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-6236744,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-6289435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-6309410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-6310132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-6413170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1648729-6442354
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6102-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1648729-Amino Acid Sequence,
pubmed-meshheading:1648729-Animals,
pubmed-meshheading:1648729-Base Sequence,
pubmed-meshheading:1648729-Cloning, Molecular,
pubmed-meshheading:1648729-DNA Transposable Elements,
pubmed-meshheading:1648729-Diptera,
pubmed-meshheading:1648729-Drosophila melanogaster,
pubmed-meshheading:1648729-Gene Library,
pubmed-meshheading:1648729-Molecular Sequence Data,
pubmed-meshheading:1648729-Nucleotidyltransferases,
pubmed-meshheading:1648729-Restriction Mapping,
pubmed-meshheading:1648729-Sequence Homology, Nucleic Acid,
pubmed-meshheading:1648729-Transposases
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pubmed:year |
1991
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pubmed:articleTitle |
A P element of Scaptomyza pallida is active in Drosophila melanogaster.
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pubmed:affiliation |
Dynamique du Génome et Evolution, Université P. et M. Curie, Paris, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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